Immunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venom

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dc.contributor.author Fernandes, I.
dc.contributor.author Assumpcao, G. G.
dc.contributor.author Silveira, C. R. F.
dc.contributor.author Faquim-Mauro, E. L.
dc.contributor.author Tanjoni, I.
dc.contributor.author Carmona, A. K. [UNIFESP]
dc.contributor.author Alves, M. F. M. [UNIFESP]
dc.contributor.author Takehara, H. A.
dc.contributor.author Rucavado, A.
dc.contributor.author Ramos, O. H. P.
dc.contributor.author Moura-da-Silva, A. M.
dc.contributor.author Gutierrez, J. M.
dc.date.accessioned 2016-01-24T14:05:39Z
dc.date.available 2016-01-24T14:05:39Z
dc.date.issued 2010-11-01
dc.identifier http://dx.doi.org/10.1016/j.toxicon.2010.07.014
dc.identifier.citation Toxicon. Oxford: Pergamon-Elsevier B.V., v. 56, n. 6, p. 1059-1065, 2010.
dc.identifier.issn 0041-0101
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/33049
dc.description.abstract BaP1 is a P-I class of Snake Venom Metalloproteinase (SVMP) relevant in the local tissue damage associated with envenomations by Bothrops asper, a medically-important species in Central America and parts of South America. Six monoclonal antibodies (MoAb) against BaP1 (MABaP1) were produced and characterized regarding their isotype, dissociation constant (K(d)), specificity and ability to neutralize BaP1-induced hemorrhagic and proteolytic activity. Two MABaP1 are IgM, three are IgG1 and one is IgG2b. the K(d)s of IgG MoAbs were in the nM range. All IgG MoAbs recognized conformational epitopes of BaP1 and B. asper venom components but failed to recognize venoms from 27 species of Viperidae, Colubridae and Elapidae families. Clone 7 cross-reacted with three P-I SVMPs tested (moojeni protease, insularinase and neuwiedase). BaP1-induced hemorrhage was totally neutralized by clones 3, 6 and 8 but not by clone 7. Inhibition of BaP1 enzymatic activity on a synthetic substrate by MABaP1 was totally achieved by clones 3 and 6, and partially by clone 8, but not by clone 7. in conclusion, these neutralizing MoAbs against BaP1 may become important tools to understand structure-function relationships of BaP1 and the role of P-I class SVMP in snakebite envenomation.(C) 2010 Elsevier B.V. All rights reserved. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship PAP (FUNDAP)
dc.description.sponsorship Vicerrectoria de Investigacion (Universidad de Costa Rica), NeTropica
dc.format.extent 1059-1065
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Toxicon
dc.rights Acesso restrito
dc.subject Monoclonal antibodies en
dc.subject Metalloproteinase en
dc.subject BaP1 en
dc.subject Hemorrhage en
dc.subject Snake venom en
dc.subject Neutralizing antibody en
dc.title Immunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venom en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Inst Butantan
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Costa Rica
dc.description.affiliation Inst Butantan, Lab Imunopatol, BR-05503900 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.affiliation Univ Costa Rica, Fac Microbiol, Inst Clodomiro Picado, San Jose, Costa Rica
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.identifier.doi 10.1016/j.toxicon.2010.07.014
dc.description.source Web of Science
dc.identifier.wos WOS:000282253900023



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